| Tag | Content |
|---|
| CPLM ID | CPLM-011831 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bifunctional protein RIB2 |
Protein Synonyms/Alias | tRNA pseudouridine(32) synthase, cytoplasmic; tRNA pseudouridine synthase 8; tRNA pseudouridylate synthase 8; tRNA-uridine isomerase 8; Diaminohydroxyphosphoribosylaminopyrimidine deaminase; DRAP deaminase; Riboflavin-specific deaminase |
Gene Name | RIB2 |
Gene Synonyms/Alias | PUS8; YOL066C |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 89 | EPYFFTYKTFCKERW | acetylation | [1] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | Responsible for synthesis of pseudouridine from uracil- 32 in cytoplasmic transfer RNAs. |
Sequence Annotation | DOMAIN 99 168 S4 RNA-binding.
REGION 1 432 tRNA pseudouridine synthase.
REGION 433 591 DRAP deaminase.
ACT_SITE 211 211 By similarity.
ACT_SITE 484 484 Proton donor (By similarity).
METAL 482 482 Zinc; catalytic (By similarity).
METAL 515 515 Zinc; catalytic (By similarity).
METAL 525 525 Zinc; catalytic (By similarity). |
Keyword | Complete proteome; Cytoplasm; Hydrolase; Isomerase; Metal-binding; Reference proteome; Riboflavin biosynthesis; RNA-binding; tRNA processing; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 591 AA |
Protein Sequence | MEDSNNEASD DFNNLLNKEI ESAKEVKLRK FANRNNNRNE NSSKVKDASG FRLRVIQTDG 60
HKTKKTDPDY EVTIDGPLRK IEPYFFTYKT FCKERWRDRK LVDVFVSEFR DREPSYYSKT 120
IAEGKVYLND EPANLDTIIR DGDLITHKVH RHEPPVTSKP IDIVFEDEDI LVIDKPSSIP 180
VHPTGRYRFN TITKMLERQL GYSVHPCNRL DKPTSGLMFL AKTPLGADRM GDQMKAREVT 240
KEYVARVKGE FPIGIVEVDK PVRSVNPKVA LNAVCEMSDE NAKHAKTVFQ RVSYDGQTSI 300
VKCKPLTGRT HQIRVHLQYL GFPIANDPIY SNPDIWGPDL GRGGLQNYDD IVLKLDAIGK 360
TNPAESWIHP HSEGEYLLGR QCEECEAEMY TDPGTNDLDL WLHAFRYESL ERNSDTQKPL 420
WSYRTKYPEW ALEPHRRYME MAVKEAGKCG PTKTAFSVGA VLVHGTQVLA TGYSRELPGN 480
THAEQCALIK YSQLHPNCPT IVPMGTVLYT TMEPCSFRLS GNEPCCDRIL ATQGAIGTVF 540
VGVMEPDTFV KNNTSLNKLE SHGVNYIQIP GYEEECTIIA FKGHDNSDDK A 591 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:SGD. GO:0043723; F:2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate deaminase activity; IMP:SGD. GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:EC. GO:0009982; F:pseudouridine synthase activity; IDA:SGD. GO:0003723; F:RNA binding; IEA:UniProtKB-KW. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0009231; P:riboflavin biosynthetic process; IMP:SGD. GO:0031119; P:tRNA pseudouridine synthesis; IMP:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |